Identification of a ten-amino acid proline-rich SH3 binding site
Abstract
The Src homology 3 (SH3) region is a small protein domain present in a very large group of proteins, including cytoskeletal elements and signaling proteins. It is believed that SH3 domains serve as modules that mediate protein-protein associations and, along with Src homology 2 (SH2) domains, regulate cytoplasmic signaling. The SH3 binding sites of two SH3 binding proteins were localized to a nine- or ten-amino acid stretch very rich in proline residues. Similar SH3 binding motifs exist in the formins, proteins that function in pattern formation in embryonic limbs of the mouse, and one subtype of the muscarinic acetylcholine receptor. Identification of the SH3 binding site provides a basis for understanding the interaction between the SH3 domains and their targets.
Additional Information
© 1993 American Association for the Advancement of Science. Received 20 October 1992; accepted 21 December 1992. We thank W. Li and A. G. Batzer in J. Schlessinger's laboratory for providing the GST-GRB2 and GST-Nck fusion proteins. Supported by a postdoctoral fellowship from the Cancer Research Institute (R.R.), National Research Service award CA 08875 (B.J.M.), National Research Service award CA 09673 (P.C.), B. Duke Glenn Fellowship (P.C.), and U.S. Public Health Service grant CA 51462 (D.B.) The first two authors contributed equally to this work.Additional details
- Eprint ID
- 103189
- DOI
- 10.1126/science.8438166
- Resolver ID
- CaltechAUTHORS:20200513-151928911
- Cancer Research Institute
- CA08875
- NIH
- CA09673
- NIH
- B. Duke Glenn Fellowship
- CA51462
- NIH
- Created
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2020-05-13Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field